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Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy
Open accessAbstract
Significance: Circular dichroism (CD) spectroscopy is widely used for protein secondary structure analysis. However, quantitative estimation for β-sheet–containing proteins is problematic due to the huge morphological and spectral diversity of β-structures. We show that parallel/antiparallel orientation and twisting of β-sheets account for the observed spectral diversity. Taking into account the twist of β-structures, our method accurately estimates the secondary structure for a broad range of protein folds, particularly for β-sheet–rich proteins and amyloid fibrils. Moreover, the method can predict the protein fold down to the topology level following the CATH classification. We provide a general tool for a quick and reliable structure analysis using conventional or synchrotron radiation CD spectroscopy, which is especially useful when X-ray or NMR techniques fail.
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Metadata
- Authors
- Micsonai, A., Wien, F., Kernya, L., Lee, Y.-H., Goto, Y., Réfrégiers, M., & Kardos, J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2015-06-02
- Volume
- 112
- Issue
- 24
- Pages
- E3095-103
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1588979652
- Cited by
- 1,703
- References
- 3
- FWCI
- 41.81
- Type
- journal article
- Language
- en
- Open access
- bronze
- Funders
- Országos Tudományos Kutatási Alapprogramok (81950)
- Hungarian National Research, Development and Innovation Office (KTIA_NAP_13-2-2014-0017)
- SOLEIL Synchrotron (20140646, 20130475, 20120589, 201110054, 20110405)
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